Research in this laboratory is centered around solution studies on the structure and dynamics of proteins, protein-protein complexes and protein-nucleic acid complexes using multidimensional NMR spectroscopy, and on the development and application of novel NMR and computational methods to aid in these studies. We have devoted significant efforts towards detecting, characterizing and visualizing highly transient, lowly-populated states that are invisible to conventional biophysical and structural techniques, yet play a key role in numerous biological processes including recognition, allostery, signal transduction, etc.... by means of paramagnetic relaxation enhancement (PRE) and novel relaxation methods, including Dark state exchange saturation transfer spectroscopy recently developed in our laboratory. Using these approaches we have been able to characterize sliding and hopping of a multidomain transcription factor on NDA, to characteristics the mechanistic details involving encounter complex formation in protein-protein interactions, and to study the exchange between monomeric and protofibril forms of amyloid Abeta, and to study the interactions of intrinsically disordered polypeptides with the chaperonin GroEL.